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  • 1
    Electronic Resource
    Electronic Resource
    Sucrose enhances the recovery and activity of ribonuclease A during reversed micelle extraction (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 58 (1998), S. 374-379 
    Details
    ISSN: 0006-3592
    Keywords: reversed micelles ; ribonuclease A ; activity ; recovery ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: We have investigated the effect of two simple sugars, glucose and sucrose, on the extraction of ribonuclease A by AOT-isooctane reversed micelles. Including the sugars at concentrations up to 0.75 M in the feed solution resulted in moderate improvements in the forward transfer efficiency. The greatest effects were seen observed in the backward transfer step where both the protein recovery yield and the activity of the protein were greatly increased. Protein transfer and activity yields were also dependent on the AOT concentration. We suggest that the presence of sucrose, which was solubilized into the reversed micelles, results in preferential hydration of ribonuclease A, reducing the protein-surfactant interactions. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:374-379, 1998.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Protein refolding at high concentration using size-exclusion chromatography (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 50 (1996), S. 16-23 
    Details
    ISSN: 0006-3592
    Keywords: protein refolding ; size-exclusion chromatography ; SEPROS ; lysozyme ; bovine carbonic anhydrase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A new method to improve refolding yields and to increase the concentration of refolded proteins in a single operation has been developed. The method uses size-exclusion chromatography matrices to perform buffer exchange, aggregate removal, and the folding reaction. The reduced diffusion of proteins in gel-filtration media has been shown to suppress the nonspecific interactions of partially folded molecules, thus reducing aggregation. Hen egg white lysozyme (HEWL) and bovine carbonic anhydrase (CAB) were successfully refolded from initial protein concentrations of up to 80 mg/mL using Sephacryl S-100 (HR). The aggregation reaction for lysozyme was reduced and was only detected at the highest protein concentration used. The average recovery of lysozyme was 63%, with an average specific activity of 104%. Carbonic anhydrase experiments also showed that aggregation was suppressed and the average protein recovery from the column was 56%, with a specific activity of 81%. This process enables refolding and the purification of active species to be achieved in a single step. © 1996 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
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